SULM – Schweizerische Union für Labormedizin | Union Suisse de Médecine de Laboratoire | Swiss Union of Laboratory Medicine

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Serenay Elgun1 , Demet Karnak2

1Dept. of Biochemistry,Ankara University School of Medicine, Ankara Turkey., 2Dept. of Chest Diseases, Ankara University School of Medicine, Ankara Turkey.

Objective: DPPIV, is involved in diverse biologic functions such as peptide-mediated cellular growth and differentiation(1). ADA, which catalyses the hydrolysis of adenosine interferes with the inhibition of T cell ability to kill tumor cells (2). Both enzymes are known to have soluble counterparts. We measured serum and pleural ADA and DPPIV activities in patients with pleural effusion due to lung cancer to determine whether these T cell associated enzymes play part in the disease mechanism and have any diagnostic value.
Methods: Pleural fluid samples obtained by thoracentesis and sera from 12 patients with lung cancer were used for ADA and DPPIV activity determination (3,4). Results were compared with those of 18 tuberculosis patients and 12 patients with congestive heart failure (CHF).
Results: Pleural and serum ADA and DPPIV activities of lung cancer group was found to be significantly decreased when compared to tuberculosis group, while no significant differences were obtained regarding the CHF group. The cut-off levels of pleural ADA and DPPIV, serum ADA and DPPIV were established. Sensitivity and specificity of pleural ADA and DPPIV measurements were found to be significant.
Summary and Conclusion: Both enzymes appear to be ‘locally expressed’ in pleural fluid. Decreased pleural and serum DPPIV and ADA activities is a further support for their association which is important for T cell activation. Lowered activities of these enzymes suggest a possible dysfunction of T cells in targeting and killing tumor cells. In addition, both enzymes seem to be reliable tests in distinguishing lung cancer from tuberculosis.
References:
1.Wesley UV, Tiwari S, Houghton AN. Int J Cancer 2004;109:855-66.
2.Blay J, White TD, Hoskin DW. Cancer Res 1997;57:2602-5.
3.Giusti G, Galanti B. In: Bergmeyer UH, ed. Methods of enzymatic analysis. Weinheim: Verlag Chemie, 1984:315-23.
4.Nagatsu T, Hino M, Fuyamada H, Hayakawa T, Sakibara S, Nakagawa Y et al. Anal Biochem 1976 ;74 :466-76.

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